UniProt functional annotation for P06632



	UniProt functional annotation for P06632

UniProt code: P06632.

Organism: Corynebacterium sp. (strain ATCC 31090).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; Corynebacterium; unclassified Corynebacterium.

Function: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.

Catalytic activity: Reaction=2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH; Xref=Rhea:RHEA:35111, ChEBI:CHEBI:11449, ChEBI:CHEBI:15378, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.346;

Activity regulation: Inhibited by Zn(2+), Fe(3+), Cu(2+) and Ni(2+).

Biophysicochemical properties: Kinetic parameters: KM=26 mM for 2,5-diketo-D-gluconate {ECO:0000269|PubMed:3597405}; KM=10 uM for NADPH {ECO:0000269|PubMed:3597405}; pH dependence: Optimum pH is 6.4. Active over a broad pH range. {ECO:0000269|PubMed:3597405};

Subunit: Monomer. {ECO:0000269|PubMed:14718658}.

Subcellular location: Cytoplasm.

Biotechnology: Introduced by genetic manipulation and expressed in Erwinia herbicola by Anderson et al. The resultant organism is able to convert in a single fermentative step D-glucose into 2-keto-L-gulonic acid, a key precursor in the industrial production of L-ascorbic acid (vitamin C). However, the technology still needs some working on and is not used in commercial production at present.

Miscellaneous: Modeling study indicates that the active site may not be optimized for 2,5-diketo-D-gluconic acid.

Similarity: Belongs to the aldo/keto reductase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Corynebacterium sp. (strain ATCC 31090).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; Corynebacterium; unclassified Corynebacterium.



Function:		Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.


Catalytic activity:		Reaction=2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH; Xref=Rhea:RHEA:35111, ChEBI:CHEBI:11449, ChEBI:CHEBI:15378, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.346;
Activity regulation:		Inhibited by Zn(2+), Fe(3+), Cu(2+) and Ni(2+).
Biophysicochemical properties:		Kinetic parameters: KM=26 mM for 2,5-diketo-D-gluconate {ECO:0000269\|PubMed:3597405}; KM=10 uM for NADPH {ECO:0000269\|PubMed:3597405}; pH dependence: Optimum pH is 6.4. Active over a broad pH range. {ECO:0000269\|PubMed:3597405};
Subunit:		Monomer. {ECO:0000269\|PubMed:14718658}.
Subcellular location:		Cytoplasm.
Biotechnology:		Introduced by genetic manipulation and expressed in Erwinia herbicola by Anderson et al. The resultant organism is able to convert in a single fermentative step D-glucose into 2-keto-L-gulonic acid, a key precursor in the industrial production of L-ascorbic acid (vitamin C). However, the technology still needs some working on and is not used in commercial production at present.
Miscellaneous:		Modeling study indicates that the active site may not be optimized for 2,5-diketo-D-gluconic acid.
Similarity:		Belongs to the aldo/keto reductase family. {ECO:0000305}.